Modification of Glutenin and Associated Changes in Digestibility Due to Methylglyoxal during Heat Processing
Modification of Glutenin and Associated Changes in Digestibility Due to Methylglyoxal during Heat Processing
复制标题
热处理过程中甲基乙二醛对谷蛋白的改性和消化率的相关变化
DOI：
10.1021/acs.jafc.9b04337
复制
发表时间：
2019-09-25
影响因子：
6.1
通讯作者：
Wang, Shuo
中科院分区：
文献类型：
--
作者：
Wang, Yaya;Wang, Junping;Wang, Shuo
麦谷蛋白是面粉中的主要蛋白质，是人类非常重要的蛋白质营养来源。甲基乙二醛（MGO）是面制品热加工过程中发生的美拉德反应的重要产物，它与麦谷蛋白反应，促进麦谷蛋白性质的变化。在这里，MGO对麦谷蛋白消化在加热过程中的影响进行了研究，使用模拟MGO-麦谷蛋白系统。MGO显著降低谷蛋白的消化率。研究了MGO-麦谷蛋白的结构和理化性质，以了解消化率下降的机制。这些数据表明，消化率的变化是由表面疏水性的降低和二硫键的增加引起的。MGO在加热后诱导麦谷蛋白的强烈聚集，这导致蛋白酶切割位点的掩蔽。此外，由MGO诱导的羰基氧化导致麦谷蛋白的分子间交联，其越来越多地掩盖甚至破坏裂解位点，进一步降低消化率。
Glutenin is the main protein of flour and is a very important source of protein nutrition for humans. Methylglyoxal (MGO) is an important product of the Maillard reaction that occurs during the hot-processing of flour products, and it reacts with glutenin to facilitate changes in glutenin properties. Here, the effects of MGO on glutenin digestion during the heating process were investigated using a simulated MGO-glutenin system. MGO significantly reduced the digestibility of glutenin. The structure of MGO-glutenin and physicochemical properties were studied to understand the mechanism of the decrease of digestibility. These data suggest that changes in digestibility were caused by decreases in surface hydrophobicity and increases in disulfide bonds. MGO induces strong aggregation of glutenin after heating that led to the masking of cleavage sites for proteases. Moreover, carbonyl oxidation induced by MGO leads to intermolecular cross-linking of glutenin that increasingly masks or even destroys cleavage sites, further decreasing digestibility.